eF-site ID 4ow3-A PDB Code 4ow3 Chain A click to enlarge Title Thermolysin structure determined by free-electron laser Classification HYDROLASE Compound Thermolysin Source ORGANISM_SCIENTIFIC: Bacillus thermoproteolyticus; Sequence A:  ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIF TYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVT YDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSQM VYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNE SGAINEAISDIFGTLVEFYANPDWEIGEDVYTPGISGDSL RSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAY LISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFS QLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK Description Functional site 1) chain A residue 142 type sequence H description binding site for residue ZN A 401 source : AC1 2) chain A residue 146 type sequence H description binding site for residue ZN A 401 source : AC1 3) chain A residue 166 type sequence E description binding site for residue ZN A 401 source : AC1 4) chain A residue 138 type sequence D description binding site for residue CA A 402 source : AC2 5) chain A residue 177 type sequence E description binding site for residue CA A 402 source : AC2 6) chain A residue 185 type sequence D description binding site for residue CA A 402 source : AC2 7) chain A residue 187 type sequence E description binding site for residue CA A 402 source : AC2 8) chain A residue 190 type sequence E description binding site for residue CA A 402 source : AC2 9) chain A residue 57 type sequence D description binding site for residue CA A 403 source : AC3 10) chain A residue 59 type sequence D description binding site for residue CA A 403 source : AC3 11) chain A residue 61 type sequence Q description binding site for residue CA A 403 source : AC3 12) chain A residue 193 type sequence Y description binding site for residue CA A 404 source : AC4 13) chain A residue 194 type sequence T description binding site for residue CA A 404 source : AC4 14) chain A residue 197 type sequence I description binding site for residue CA A 404 source : AC4 15) chain A residue 200 type sequence D description binding site for residue CA A 404 source : AC4 16) chain A residue 177 type sequence E description binding site for residue CA A 405 source : AC5 17) chain A residue 183 type sequence N description binding site for residue CA A 405 source : AC5 18) chain A residue 185 type sequence D description binding site for residue CA A 405 source : AC5 19) chain A residue 190 type sequence E description binding site for residue CA A 405 source : AC5 20) chain A residue 143 type ACT_SITE sequence E description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:4808703 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 231 type ACT_SITE sequence H description Proton donor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:4808703 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 139-148 type prosite sequence VVAHELTHAV description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELTHAV source prosite : PS00142 23) chain A residue 142 type catalytic sequence H description 176 source MCSA : MCSA1 24) chain A residue 143 type catalytic sequence E description 176 source MCSA : MCSA1 25) chain A residue 146 type catalytic sequence H description 176 source MCSA : MCSA1 26) chain A residue 157 type catalytic sequence Y description 176 source MCSA : MCSA1 27) chain A residue 166 type catalytic sequence E description 176 source MCSA : MCSA1 28) chain A residue 226 type catalytic sequence D description 176 source MCSA : MCSA1 29) chain A residue 231 type catalytic sequence H description 176 source MCSA : MCSA1 30) chain A residue 185 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 31) chain A residue 187 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 32) chain A residue 190 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 33) chain A residue 193 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 34) chain A residue 194 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 35) chain A residue 197 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI3 36) chain A residue 200 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 37) chain A residue 61 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI3 38) chain A residue 138 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 39) chain A residue 142 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 40) chain A residue 146 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI3 41) chain A residue 166 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 42) chain A residue 177 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 43) chain A residue 183 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 44) chain A residue 57 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 45) chain A residue 59 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3

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